Insulin increases membrane and cytosolic protein kinase C activity in BC3H-1 myocytes.
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Early insulin-induced increases in membrane and cytosolic protein kinase C activity may be related to increased diacylglycerol generation from de novo phosphatidic acid synthesis, as there were rapid increases in [3H] Glycerol incorporation into diacyLglycerols at later, as well as very early time points.About:
This article is published in Journal of Biological Chemistry.The article was published on 1987-03-15 and is currently open access. It has received 160 citations till now. The article focuses on the topics: Protein kinase C & cGMP-dependent protein kinase.read more
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Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B.
TL;DR: Data indicate that insulin rapidly causes inactivation of GSK-3 and that this is due to phosphorylation of G SK-3, which has implications for the control of glycogen and protein metabolism.
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Glucose Transport and Glucose Transporters in Muscle and Their Metabolic Regulation
Amira Klip,Michel R Pâquet +1 more
TL;DR: In rat skeletal muscle, acute treatment with insulin in vivo increases glucose-transport activity and the number of specific cytochalasin B-binding sites at the plasma membrane, and in mildly diabetic (streptozocin-induced) rats, the expression of the GLUT-1 glucose transporter is modulated by insulin.
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Insulin Rapidly Increases Diacylglycerol by Activating De Novo Phosphatidic Acid Synthesis
Robert V. Farese,Thomas Suman Konda,John S. Davis,Mary L. Standaert,R J Pollet,Denise R. Cooper +5 more
TL;DR: Both phospholipid effects of insulin seem important for generating diacylglycerol and other phospholipsid-derived intracellular signaling substances.
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In vitro studies on the action of CS-045, a new antidiabetic agent.
Theodore P. Ciaraldi,Allison Gilmore,Allison Gilmore,Jerrold M. Olefsky,Jerrold M. Olefsky,Michelle Goldberg,Michelle Goldberg,Kim A. Heidenreich,Kim A. Heidenreich +8 more
TL;DR: It is concluded that CS-045 may act directly on muscle and liver cells to increase glucose utilization and be effective in reducing glucose production, and may account in part for the ability ofCS-045 to reduce blood sugar levels in vivo.
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Differential acute and chronic response of protein kinase C in cultured neonatal rat heart myocytes to α1-adrenergic and phorbol ester stimulation ☆
TL;DR: Both acute activation and chronic regulation of PKC by NE and PMA were compared in cultured neonatal rat heart myocytes, finding that acute PKC activation by PMA was more pronounced and persistent than that by NE.
References
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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
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The role of protein kinase C in cell surface signal transduction and tumour promotion
TL;DR: Protein kinase C probably serves as a receptor for the tumour promoters and further exploration of the roles of this enzyme may provide clues for understanding the mechanism of cell growth and differentiation.
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Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters
TL;DR: Kinetic analysis indicates that TPA can substitute for diacylglycerol and greatly increases the affinity of the enzyme for Ca2+ as well as for phospholipid, and various phorbol derivatives which have been shown to be active in tumor promotion are also capable of activating this protein kinase in in vitro systems.
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Phorbol esters increase the amount of Ca2+, phospholipid-dependent protein kinase associated with plasma membrane.
TL;DR: Treatment of parietal yolk sacs cells with biologically active 12-O-tetradecanoyl phorbol-13-acetate (TPA) provokes a rapid decrease in cytosolic Ca,PL-PK activity that is accompanied by a significant increase in the amount of Ca, PL- PK activity associated with the plasma membrane fraction.
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Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover.
TL;DR: A possible coupling is proposed between the protein kinase activation and phosphatidylinositol turnover which can be provoked by various extracellular messengers.